Iron in PDB 4m6y: Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid

The structure of Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid, PDB code: 4m6y was solved by Y.C.Liu, X.W.Zou, H.C.Chan, C.J.Huang, T.L.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.34 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.160, 89.626, 136.622, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 25.5

The structure of Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Iron atom in the Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid (pdb code 4m6y). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid, PDB code: 4m6y:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe403 b:46.4 occ:1.00 OAK A:56D402 2.2 45.0 1.0 NE2 A:HIS295 2.3 38.0 1.0 NE2 A:HIS243 2.4 38.9 1.0 OAM A:56D402 2.5 50.1 1.0 O1 A:OXY408 2.5 48.8 1.0 O2 A:OXY408 2.7 42.4 1.0 CAH A:56D402 2.8 48.9 1.0 CAI A:56D402 3.0 49.5 1.0 CE1 A:HIS295 3.2 38.6 1.0 CE1 A:HIS243 3.2 37.5 1.0 CD2 A:HIS295 3.4 39.7 1.0 CD2 A:HIS243 3.4 36.7 1.0 OAL A:56D402 4.2 52.6 1.0 CAG A:56D402 4.2 51.4 1.0 ND1 A:HIS295 4.4 39.6 1.0 ND1 A:HIS243 4.4 35.9 1.0 CG A:HIS243 4.5 34.8 1.0 CG A:HIS295 4.5 38.1 1.0 CAJ A:56D402 4.6 52.2 1.0 CE1 A:PHE291 4.7 29.7 1.0 CD2 A:LEU244 4.8 44.7 1.0 CAE A:56D402 4.8 49.5 1.0 O A:HOH695 4.9 51.3 1.0 CG A:LEU244 4.9 46.1 1.0 CAD A:56D402 5.0 49.2 1.0

Iron binding site 2 out of 2 in the Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Mutant Structure of Methyltransferase From Streptomyces Hygroscopicus Complexed with S-Adenosyl-L-Homocysteine and Methylphenylpyruvic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe403 b:55.3 occ:1.00 OAK B:56D402 2.2 58.4 1.0 NE2 B:HIS295 2.3 46.3 1.0 O1 B:OXY406 2.4 57.0 1.0 O2 B:OXY406 2.4 58.7 1.0 NE2 B:HIS243 2.5 60.6 1.0 OAL B:56D402 2.6 67.8 1.0 CE1 B:HIS295 3.0 47.9 1.0 CAH B:56D402 3.0 61.1 1.0 CAI B:56D402 3.2 61.7 1.0 CD2 B:HIS243 3.2 58.8 1.0 CD2 B:HIS295 3.4 44.5 1.0 CE1 B:HIS243 3.6 59.5 1.0 CD1 B:LEU244 4.0 67.0 1.0 ND1 B:HIS295 4.2 47.9 1.0 OAM B:56D402 4.4 59.5 1.0 CG B:HIS243 4.4 60.2 1.0 CG B:HIS295 4.4 46.1 1.0 CAG B:56D402 4.4 62.8 1.0 CE1 B:PHE291 4.5 44.3 1.0 ND1 B:HIS243 4.6 59.8 1.0 O B:HOH620 4.7 64.6 1.0 CAJ B:56D402 4.9 66.5 1.0 CAE B:56D402 4.9 62.5 1.0 CZ B:PHE291 4.9 47.0 1.0

X.W.Zou, Y.C.Liu, N.S.Hsu, C.J.Huang, S.Y.Lyu, H.C.Chan, C.Y.Chang, H.W.Yeh, K.H.Lin, C.J.Wu, M.D.Tsai, T.L.Li. Structure and Mechanism of A Nonhaem-Iron Sam-Dependent C-Methyltransferase and Its Engineering to A Hydratase and An O-Methyltransferase Acta Crystallogr.,Sect.D V. 70 1549 2014.
ISSN: ISSN 0907-4449
PubMed: 24914966
DOI: 10.1107/S1399004714005239